BioDesign 2020; 8(4): 93-98
Published online December 30, 2020
© Korean Society for Structural Biology
Do-Heon Gu1, Cheolsoo Eo2, Dong Tak Jeong2, Jeong-Sun Kim1 and Suk-Youl Park2,*
1Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea
2Pohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea
Correspondence to: firstname.lastname@example.org
Serial crystallography (SX) makes a significant contribution for time-resolved studies and forms the base of structural analysis at room temperature, with minimal radiation damage. Even though X-ray free electron laser provides a femtosecond scale X-ray pulse, high accessibility of synchrotron facilities gives a merit for application of SX experiment. Therefore, we performed serial synchrotron crystallography (SSX) of lysozyme crystals at room-temperature. Both fixed target and injector-based methods were used for SX experiments to determine the structure of lysozyme crystals. Approximately 19,600 and 40,000 diffraction images were collected during 40 and 80 min, for fixed target and injectionbased methods, respectively in the SSX experiments. The 10 Hz synchrotron X-ray radiation of the 11C beamline of the Pohang accelerator laboratory was used and the crystal structures of lysozyme were determined at 1.89 Å and 1.80 Å resolutions, respectively. These results provide experimental clues for routine SX at room temperature in synchrotrons.